Preprint Communication Version 1 Preserved in Portico This version is not peer-reviewed

Exploring the Interaction of E3 Ubiquitin-Protein Ligase Parkin with Natural Compound Amentoflavone: Implications for Parkinson’s Disease Therapy

Version 1 : Received: 21 January 2024 / Approved: 23 January 2024 / Online: 23 January 2024 (07:47:32 CET)

How to cite: Ferrari, I.V. Exploring the Interaction of E3 Ubiquitin-Protein Ligase Parkin with Natural Compound Amentoflavone: Implications for Parkinson’s Disease Therapy. Preprints 2024, 2024011652. https://doi.org/10.20944/preprints202401.1652.v1 Ferrari, I.V. Exploring the Interaction of E3 Ubiquitin-Protein Ligase Parkin with Natural Compound Amentoflavone: Implications for Parkinson’s Disease Therapy. Preprints 2024, 2024011652. https://doi.org/10.20944/preprints202401.1652.v1

Abstract

Parkinson's disease is a neurodegenerative disorder resulting from progressive damage to specific brain regions. Key symptoms encompass involuntary movements (tremor), slowness of movements (bradykinesia), and muscle rigidity. Although the precise cause remains uncertain, a combination of genetic and environmental factors is believed to contribute to its development. This study focuses on the interaction of the E3 ubiquitin-protein ligase parkin with natural compounds. Docking investigations revealed that Amentoflavone exhibited an excellent binding energy score of approximately -10 kcal/mol. The E3 ubiquitin-protein ligase parkin displayed a robust binding affinity with docked amentoflavone, evident from a high binding energy of -10 kcal/mol. Nonetheless, additional biological studies are crucial not only to validate its potential efficacy against Parkinson's and assess safety in terms of toxicity but also to perform further computational analyses confirming these preliminary assessments.

Keywords

docking studies; amentoflavone; Parkinson's disease; pyrx program

Subject

Biology and Life Sciences, Neuroscience and Neurology

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